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P19971

- TYPH_HUMAN

UniProt

P19971 - TYPH_HUMAN

Protein

Thymidine phosphorylase

Gene

TYMP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro.1 Publication
    Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.1 Publication

    Catalytic activityi

    Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei116 – 1161Substrate
    Binding sitei202 – 2021Substrate
    Binding sitei217 – 2171Substrate
    Binding sitei221 – 2211Substrate

    GO - Molecular functioni

    1. phosphorylase activity Source: InterPro
    2. platelet-derived growth factor receptor binding Source: ProtInc
    3. pyrimidine-nucleoside phosphorylase activity Source: InterPro
    4. thymidine phosphorylase activity Source: ProtInc
    5. transferase activity, transferring pentosyl groups Source: Reactome

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. chemotaxis Source: UniProtKB-KW
    4. DNA replication Source: ProtInc
    5. mitochondrial genome maintenance Source: ProtInc
    6. nucleobase-containing small molecule metabolic process Source: Reactome
    7. pyrimidine nucleobase metabolic process Source: Reactome
    8. pyrimidine nucleoside catabolic process Source: Reactome
    9. pyrimidine nucleoside salvage Source: Reactome
    10. pyrimidine nucleotide metabolic process Source: ProtInc
    11. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Developmental protein, Glycosyltransferase, Growth factor, Transferase

    Keywords - Biological processi

    Angiogenesis, Chemotaxis, Differentiation

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00442-MONOMER.
    BRENDAi2.4.2.4. 2681.
    ReactomeiREACT_1023. Pyrimidine catabolism.
    REACT_655. Pyrimidine salvage reactions.
    SABIO-RKP19971.
    UniPathwayiUPA00578; UER00638.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thymidine phosphorylase (EC:2.4.2.4)
    Short name:
    TP
    Alternative name(s):
    Gliostatin
    Platelet-derived endothelial cell growth factor
    Short name:
    PD-ECGF
    TdRPase
    Gene namesi
    Name:TYMP
    Synonyms:ECGF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:3148. TYMP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Mitochondrial DNA depletion syndrome 1, MNGIE type (MTDPS1) [MIM:603041]: A multisystem disease associated with mitochondrial dysfunction. It is clinically characterized by onset between the second and fifth decades of life, ptosis, progressive external ophthalmoplegia, gastrointestinal dysmotility (often pseudoobstruction), diffuse leukoencephalopathy, cachexia, peripheral neuropathy, and myopathy.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441R → Q in MTDPS1. 1 Publication
    VAR_016777
    Natural varianti145 – 1451G → R in MTDPS1. 1 Publication
    VAR_007643
    Natural varianti153 – 1531G → S in MTDPS1. 1 Publication
    VAR_007644
    Natural varianti222 – 2221K → R in MTDPS1. 1 Publication
    VAR_007645
    Natural varianti289 – 2891E → A in MTDPS1. 1 Publication
    VAR_007646
    Natural varianti397 – 3982Missing in MTDPS1.
    VAR_007647

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi199 – 1991Y → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi199 – 1991Y → F: Reduced catalytic activity. 1 Publication
    Mutagenesisi199 – 1991Y → L: Reduced catalytic activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Progressive external ophthalmoplegia

    Organism-specific databases

    MIMi603041. phenotype.
    Orphaneti298. Mitochondrial neurogastrointestinal encephalomyopathy.
    PharmGKBiPA162407502.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 1010PRO_0000035874
    Chaini11 – 482472Thymidine phosphorylasePRO_0000035875Add
    BLAST

    Proteomic databases

    MaxQBiP19971.
    PaxDbiP19971.
    PRIDEiP19971.

    2D gel databases

    OGPiP19971.

    PTM databases

    PhosphoSiteiP19971.

    Expressioni

    Gene expression databases

    ArrayExpressiP19971.
    BgeeiP19971.
    CleanExiHS_TYMP.
    GenevestigatoriP19971.

    Organism-specific databases

    HPAiCAB002518.
    HPA001072.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi108219. 8 interactions.
    IntActiP19971. 1 interaction.
    STRINGi9606.ENSP00000252029.

    Structurei

    Secondary structure

    1
    482
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 449
    Helixi51 – 6313
    Helixi68 – 8114
    Helixi85 – 9612
    Helixi106 – 1116
    Beta strandi112 – 1187
    Helixi125 – 13410
    Turni135 – 1373
    Beta strandi139 – 1435
    Helixi154 – 1585
    Helixi170 – 18011
    Beta strandi181 – 1855
    Beta strandi189 – 1924
    Helixi193 – 20412
    Helixi211 – 22414
    Beta strandi228 – 2369
    Beta strandi240 – 2445
    Helixi245 – 26117
    Beta strandi266 – 2727
    Beta strandi280 – 2834
    Helixi284 – 29411
    Helixi300 – 31617
    Beta strandi319 – 3224
    Helixi323 – 33513
    Helixi338 – 34912
    Helixi354 – 3629
    Helixi365 – 3717
    Beta strandi376 – 3827
    Beta strandi387 – 3926
    Helixi394 – 40512
    Beta strandi409 – 4124
    Beta strandi420 – 4234
    Beta strandi436 – 44611
    Helixi449 – 45810
    Beta strandi459 – 4646
    Beta strandi475 – 4773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UOUX-ray2.11A12-482[»]
    2J0FX-ray2.31A/B/C/D1-482[»]
    2WK5X-ray2.99A/B/C/D1-482[»]
    2WK6X-ray2.50A/B1-482[»]
    ProteinModelPortaliP19971.
    SMRiP19971. Positions 32-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19971.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati265 – 27915R-V-A-A-A-L-X(5,6)-L-G-RAdd
    BLAST
    Repeati329 – 34214R-V-A-A-A-L-X(5,6)-L-G-RAdd
    BLAST
    Repeati393 – 4019R-A-L-X-X-A-L-V-L
    Repeati453 – 4619R-A-L-X-X-A-L-V-L

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0213.
    HOGENOMiHOG000047313.
    HOVERGENiHBG000082.
    KOiK00758.
    OMAiNVGHTLE.
    OrthoDBiEOG744T97.
    PhylomeDBiP19971.
    TreeFamiTF332198.

    Family and domain databases

    Gene3Di3.40.1030.10. 1 hit.
    3.90.1170.30. 1 hit.
    InterProiIPR000312. Glycosyl_Trfase_fam3.
    IPR017459. Glycosyl_Trfase_fam3_N_dom.
    IPR013102. PYNP_C.
    IPR018090. Pyrmidine_PPas_bac/euk.
    IPR000053. Pyrmidine_PPase.
    IPR017872. Pyrmidine_PPase_CS.
    [Graphical view]
    PANTHERiPTHR10515. PTHR10515. 1 hit.
    PfamiPF02885. Glycos_trans_3N. 1 hit.
    PF00591. Glycos_transf_3. 1 hit.
    PF07831. PYNP_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000478. TP_PyNP. 1 hit.
    SMARTiSM00941. PYNP_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF47648. SSF47648. 1 hit.
    SSF52418. SSF52418. 1 hit.
    SSF54680. SSF54680. 1 hit.
    TIGRFAMsiTIGR02644. Y_phosphoryl. 1 hit.
    PROSITEiPS00647. THYMID_PHOSPHORYLASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19971-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAALMTPGTG APPAPGDFSG EGSQGLPDPS PEPKQLPELI RMKRDGGRLS    50
    EADIRGFVAA VVNGSAQGAQ IGAMLMAIRL RGMDLEETSV LTQALAQSGQ 100
    QLEWPEAWRQ QLVDKHSTGG VGDKVSLVLA PALAACGCKV PMISGRGLGH 150
    TGGTLDKLES IPGFNVIQSP EQMQVLLDQA GCCIVGQSEQ LVPADGILYA 200
    ARDVTATVDS LPLITASILS KKLVEGLSAL VVDVKFGGAA VFPNQEQARE 250
    LAKTLVGVGA SLGLRVAAAL TAMDKPLGRC VGHALEVEEA LLCMDGAGPP 300
    DLRDLVTTLG GALLWLSGHA GTQAQGAARV AAALDDGSAL GRFERMLAAQ 350
    GVDPGLARAL CSGSPAERRQ LLPRAREQEE LLAPADGTVE LVRALPLALV 400
    LHELGAGRSR AGEPLRLGVG AELLVDVGQR LRRGTPWLRV HRDGPALSGP 450
    QSRALQEALV LSDRAPFAAP SPFAELVLPP QQ 482
    Length:482
    Mass (Da):49,955
    Last modified:June 7, 2005 - v2
    Checksum:i0652FA0B8F3BDE28
    GO
    Isoform 2 (identifier: P19971-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         386-386: D → DAPLPA

    Note: No experimental confirmation available.

    Show »
    Length:487
    Mass (Da):50,405
    Checksum:iC2F16246C51DCE00
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti195 – 1951D → E in AAH18160. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441R → Q in MTDPS1. 1 Publication
    VAR_016777
    Natural varianti145 – 1451G → R in MTDPS1. 1 Publication
    VAR_007643
    Natural varianti153 – 1531G → S in MTDPS1. 1 Publication
    VAR_007644
    Natural varianti222 – 2221K → R in MTDPS1. 1 Publication
    VAR_007645
    Natural varianti289 – 2891E → A in MTDPS1. 1 Publication
    VAR_007646
    Natural varianti397 – 3982Missing in MTDPS1.
    VAR_007647
    Natural varianti471 – 4711S → L.2 Publications
    Corresponds to variant rs11479 [ dbSNP | Ensembl ].
    VAR_007648

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei386 – 3861D → DAPLPA in isoform 2. 1 PublicationVSP_045556

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63193 mRNA. Translation: AAA60043.1.
    AK225269 mRNA. No translation available.
    U62317 Genomic DNA. Translation: AAB03344.2.
    BC018160 mRNA. Translation: AAH18160.1.
    BC052211 mRNA. Translation: AAH52211.1.
    CCDSiCCDS14096.1. [P19971-1]
    CCDS58811.1. [P19971-2]
    PIRiS03904.
    RefSeqiNP_001107227.1. NM_001113755.2. [P19971-1]
    NP_001107228.1. NM_001113756.2. [P19971-1]
    NP_001244917.1. NM_001257988.1. [P19971-1]
    NP_001244918.1. NM_001257989.1. [P19971-2]
    NP_001944.1. NM_001953.4. [P19971-1]
    UniGeneiHs.180903.
    Hs.730607.

    Genome annotation databases

    EnsembliENST00000252029; ENSP00000252029; ENSG00000025708. [P19971-1]
    ENST00000395678; ENSP00000379036; ENSG00000025708. [P19971-1]
    ENST00000395680; ENSP00000379037; ENSG00000025708. [P19971-1]
    ENST00000395681; ENSP00000379038; ENSG00000025708. [P19971-2]
    GeneIDi1890.
    KEGGihsa:1890.
    UCSCiuc003bmb.5. human. [P19971-1]

    Polymorphism databases

    DMDMi67477361.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    R&D Systems' cytokine mini-reviews: PD-ECGF
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63193 mRNA. Translation: AAA60043.1 .
    AK225269 mRNA. No translation available.
    U62317 Genomic DNA. Translation: AAB03344.2 .
    BC018160 mRNA. Translation: AAH18160.1 .
    BC052211 mRNA. Translation: AAH52211.1 .
    CCDSi CCDS14096.1. [P19971-1 ]
    CCDS58811.1. [P19971-2 ]
    PIRi S03904.
    RefSeqi NP_001107227.1. NM_001113755.2. [P19971-1 ]
    NP_001107228.1. NM_001113756.2. [P19971-1 ]
    NP_001244917.1. NM_001257988.1. [P19971-1 ]
    NP_001244918.1. NM_001257989.1. [P19971-2 ]
    NP_001944.1. NM_001953.4. [P19971-1 ]
    UniGenei Hs.180903.
    Hs.730607.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UOU X-ray 2.11 A 12-482 [» ]
    2J0F X-ray 2.31 A/B/C/D 1-482 [» ]
    2WK5 X-ray 2.99 A/B/C/D 1-482 [» ]
    2WK6 X-ray 2.50 A/B 1-482 [» ]
    ProteinModelPortali P19971.
    SMRi P19971. Positions 32-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108219. 8 interactions.
    IntActi P19971. 1 interaction.
    STRINGi 9606.ENSP00000252029.

    Chemistry

    BindingDBi P19971.
    ChEMBLi CHEMBL3106.
    DrugBanki DB01101. Capecitabine.
    DB01248. Docetaxel.
    DB00322. Floxuridine.
    DB00544. Fluorouracil.
    DB00795. Sulfasalazine.
    DB00675. Tamoxifen.

    PTM databases

    PhosphoSitei P19971.

    Polymorphism databases

    DMDMi 67477361.

    2D gel databases

    OGPi P19971.

    Proteomic databases

    MaxQBi P19971.
    PaxDbi P19971.
    PRIDEi P19971.

    Protocols and materials databases

    DNASUi 1890.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252029 ; ENSP00000252029 ; ENSG00000025708 . [P19971-1 ]
    ENST00000395678 ; ENSP00000379036 ; ENSG00000025708 . [P19971-1 ]
    ENST00000395680 ; ENSP00000379037 ; ENSG00000025708 . [P19971-1 ]
    ENST00000395681 ; ENSP00000379038 ; ENSG00000025708 . [P19971-2 ]
    GeneIDi 1890.
    KEGGi hsa:1890.
    UCSCi uc003bmb.5. human. [P19971-1 ]

    Organism-specific databases

    CTDi 1890.
    GeneCardsi GC22M050964.
    GeneReviewsi TYMP.
    HGNCi HGNC:3148. TYMP.
    HPAi CAB002518.
    HPA001072.
    MIMi 131222. gene.
    603041. phenotype.
    neXtProti NX_P19971.
    Orphaneti 298. Mitochondrial neurogastrointestinal encephalomyopathy.
    PharmGKBi PA162407502.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0213.
    HOGENOMi HOG000047313.
    HOVERGENi HBG000082.
    KOi K00758.
    OMAi NVGHTLE.
    OrthoDBi EOG744T97.
    PhylomeDBi P19971.
    TreeFami TF332198.

    Enzyme and pathway databases

    UniPathwayi UPA00578 ; UER00638 .
    BioCyci MetaCyc:HS00442-MONOMER.
    BRENDAi 2.4.2.4. 2681.
    Reactomei REACT_1023. Pyrimidine catabolism.
    REACT_655. Pyrimidine salvage reactions.
    SABIO-RK P19971.

    Miscellaneous databases

    EvolutionaryTracei P19971.
    GeneWikii ECGF1.
    GenomeRNAii 1890.
    NextBioi 7707.
    PROi P19971.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19971.
    Bgeei P19971.
    CleanExi HS_TYMP.
    Genevestigatori P19971.

    Family and domain databases

    Gene3Di 3.40.1030.10. 1 hit.
    3.90.1170.30. 1 hit.
    InterProi IPR000312. Glycosyl_Trfase_fam3.
    IPR017459. Glycosyl_Trfase_fam3_N_dom.
    IPR013102. PYNP_C.
    IPR018090. Pyrmidine_PPas_bac/euk.
    IPR000053. Pyrmidine_PPase.
    IPR017872. Pyrmidine_PPase_CS.
    [Graphical view ]
    PANTHERi PTHR10515. PTHR10515. 1 hit.
    Pfami PF02885. Glycos_trans_3N. 1 hit.
    PF00591. Glycos_transf_3. 1 hit.
    PF07831. PYNP_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000478. TP_PyNP. 1 hit.
    SMARTi SM00941. PYNP_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47648. SSF47648. 1 hit.
    SSF52418. SSF52418. 1 hit.
    SSF54680. SSF54680. 1 hit.
    TIGRFAMsi TIGR02644. Y_phosphoryl. 1 hit.
    PROSITEi PS00647. THYMID_PHOSPHORYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor."
      Ishikawa F., Miyazono K., Hellman U., Drexler H., Wernstedt C., Hagiwara K., Usuki K., Takaku F., Risau W., Heldin C.-H.
      Nature 338:557-562(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT LEU-471.
      Tissue: Placenta.
    2. "Expression of recombinant platelet-derived endothelial cell growth factor in the yeast Saccharomyces cerevisiae."
      Finnis C., Goodey A., Courtney M., Sleep D.
      Yeast 8:57-60(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Dermoid cancer.
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-471.
      Tissue: Brain and Lung.
    6. Cited for: NUCLEOTIDE SEQUENCE OF 149-244, PROTEIN SEQUENCE OF 125-178 AND 236-244.
    7. "Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor."
      Asai K., Nakanishi K., Isobe I., Eksioglu Y.Z., Hirano A., Hama K., Miyamoto T., Kato T.
      J. Biol. Chem. 267:20311-20316(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    8. "Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity."
      Usuki K., Saras J., Waltenberger J., Miyazono K., Pierce G., Thomason A., Heldin C.-H.
      Biochem. Biophys. Res. Commun. 184:1311-1316(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 12-482 IN COMPLEX WITH INHIBITOR, SUBUNIT.
    11. "Structural basis for non-competitive product inhibition in human thymidine phosphorylase: implications for drug design."
      El Omari K., Bronckaers A., Liekens S., Perez-Perez M.J., Balzarini J., Stammers D.K.
      Biochem. J. 399:199-204(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), SUBUNIT.
    12. "Structures of native human thymidine phosphorylase and in complex with 5-iodouracil."
      Mitsiki E., Papageorgiou A.C., Iyer S., Thiyagarajan N., Prior S.H., Sleep D., Finnis C., Acharya K.R.
      Biochem. Biophys. Res. Commun. 386:666-670(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) ALONE AND IN COMPLEX WITH 5-IODOURACIL, SUBSTRATE-BINDING SITES, MUTAGENESIS OF TYR-199.
    13. "Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder."
      Nishino I., Spinazzola A., Hirano M.
      Science 283:689-692(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MTDPS1 ARG-145; SER-153; ARG-222; ALA-289 AND 397-LEU-ALA-398 DEL.
    14. Cited for: VARIANT MTDPS1 GLN-44.

    Entry informationi

    Entry nameiTYPH_HUMAN
    AccessioniPrimary (citable) accession number: P19971
    Secondary accession number(s): A8MW15
    , H9KVA0, Q13390, Q8WVB7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 173 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3